Yang Chao-Nan, Liu Wei, Liu Hao-Tian, Zhang Ji-Chang, Yu Ru-Jia, Ying Yi-Lun, Long Yi-Tao
State Key Laboratory of Analytical Chemistry for Life Science, School of Chemistry and Chemical Engineering, Nanjing University, Nanjing 210023, China.
Chemistry and Biomedicine Innovation Center, Nanjing University, Nanjing 210023, P.R. China.
ACS Meas Sci Au. 2023 Nov 10;4(1):76-80. doi: 10.1021/acsmeasuresciau.3c00046. eCollection 2024 Feb 21.
Reactions involving sulfhydryl groups play a critical role in maintaining the structure and function of proteins. However, traditional mechanistic studies have mainly focused on reaction rates and the efficiency in bulk solutions. Herein, we have designed a cysteine-mutated nanopore as a biological protein nanoreactor for electrochemical visualization of the thiol substitute reaction. Statistical analysis of characteristic current signals shows that the apparent reaction rate at the single-molecule level in this confined nanoreactor reached 1400 times higher than that observed in bulk solution. This substantial acceleration of thiol substitution reactions within the nanopore offers promising opportunities for advancing the design and optimization of micro/nanoreactors. Moreover, our results could shed light on the understanding of sulfhydryl reactions and the thiol-involved signal transduction mechanisms in biological systems.
涉及巯基的反应在维持蛋白质的结构和功能方面起着关键作用。然而，传统的机理研究主要集中在反应速率和本体溶液中的效率上。在此，我们设计了一种半胱氨酸突变的纳米孔作为生物蛋白质纳米反应器，用于硫醇取代反应的电化学可视化。对特征电流信号的统计分析表明，在这个受限的纳米反应器中，单分子水平的表观反应速率比在本体溶液中观察到的高出1400倍。纳米孔内硫醇取代反应的这种显著加速为推进微/纳米反应器的设计和优化提供了有前景的机会。此外，我们的结果有助于理解生物系统中的巯基反应和涉及硫醇的信号转导机制。
